Module 1 - Biology For Engineers

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Department of Biotechnology Biology for Engineers (S4CCA01)

Introduction to Biology: The cell: the basic unit of life, Structure and functions of a cell. The Plant Cell
and animal cell, Prokaryotic and Eukaryotic cell, Stem cells and their application. Biomolecules: Properties
and functions of Carbohydrates, Nucleic acids, proteins, lipids. Importance of special biomolecules;
Enzymes (Classification (with one example each), Properties and functions), vitamins and hormones.

Introduction
The basic structural and functional unit of cellular organization is the cell. Within a selective and
relative semi permeable membrane, it contains a complete set of different kinds of units necessary
to permit its own growth and reproduction from simple nutrients. All organisms, more complex than
viruses, consist of cells, yet they consist of a strand of nucleic acid, either DNA or RNA, surrounded
by a protective protein coat (the capsid). The word cell is derived from the Latin word cellula, which
means small compartment. Hooke published his findings in his famous work, Micrographia. He only
observed cell walls because cork cells are dead and without cytoplasmic contents. A.G. Loewy and P.
Siekevitz have defined cell as ―A unit of biological activity delimited by a semi permeable membrane
and capable of self-reproduction in a medium free of other living organisms‖. John Paul has defined
the cell as ―The simplest integrated organization in living systems, capable of independent survival‖.

Historical background

Ancient Greek philosophers such as Aristotle 384-322 B.C and Paracelsus concluded that ―All
animals and plants, however, complicated, are constituted of a few elements which are repeated in
each of them‖. They were referring to macroscopic structures of an organism such as roots, leaves
and flowers common to different plants, or segments and organs that are repeated in the animal
kingdom. Many centuries later, owing to the invention of magnifying lenses, the world of
microscopic dimensions was discovered. Da Vinci (1485) recommended the uses of lenses in
viewing small objects. In 1558, Swiss biologist, Conard Gesner (1516-1565) published results on his
studies on the structure of a group of protists called foraminifera. His sketches of these protozoa
included so many details that they could only have been made if he had used form of magnifying
lenses. Perhaps, this is earliest recorded use of a magnifying instrument in a biological study.
Cell theory
The generally accepted parts of modern cell theory include:
1- All known living things are made up of one or more cells.
2- All living cells arise from pre-existing cells by division.
3- The cell is the fundamental unit of structure and function in all living organisms.
4- The activity of an organism depends on the total activity of independent cells.
5- Energy flow (metabolism and biochemistry) occurs within cells.
6- Cells contain DNA which is found specifically in the chromosome and RNA found in the cell
nucleus and cytoplasm.
7-All cells are basically the same in chemical composition in organisms of similar species.

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Department of Biotechnology Biology for Engineers (S4CCA01)
The modern version of the cell theory:
The modern version of the cell theory includes the ideas that:
1- Energy flow occurs within cells.
2- Heredity information (DNA) is passed on from cell to cell.
3- All cells have the same basic chemical composition.

Size and structure of the cell

There are many cells in an individual, which performs several functions throughout the life. The
different types of cells include- prokaryotic cell, plant and animal cell (Eukaryotic cells). The size
and the shape of the cell range from millimeter to microns, which are generally based on the type
of function that it performs. A cell generally varies in their shapes. A few cells are in spherical,
rod, flat, concave, curved, rectangular, oval etc. These cells can only be seen under microscope.

Figure: The different sizes and morphologies of cell

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Department of Biotechnology Biology for Engineers (S4CCA01)

Figure : Several different types of cells all referenced to a standard E. coli ruler of 1
micron (A) The protist Giardia lamblia, (B) a plant cell, (C) a budding yeast cell, (D) a red
blood cell, (E) a fibroblast cell, (F) a nerve cell, and (G) a rod cell from the retina.

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Prokaryotic and Eukaryotic cell
Body of all living organisms except virus has cellular organization and may contain one or many
cells. The organisms with only one cell in their body are known as unicellular (bacteria, protozoa
etc.) and organisms with many cells in their body are known as multicellular organisms (most
plants and animals). Any cellular organization may contain only one type of cell from the
following types:
A- Prokaryotic cell
B- Eukaryotic cell
These terms were suggested by Hans Ris in the 1960‘s.

Prokaryotic cells
The prokaryotic (Gr., pro= primitive or before and karyon = nucleus) are small, simple, and most
primitive organisms. They are probably first to come into existence perhaps 3.5 billion years ago.
These cells occur in bacteria (i.e., Mycoplasma, Cyanobacteria etc). Prokaryotic cell is a one
envelope system organized in depth. It consists of central nuclear components surrounded by
cytoplasmic ground substance, with whole cell enveloped by a plasma membrane. The cytoplasm
of prokaryotic cell lacks nuclear envelope, any other cytoplasmic membrane and well defined
cytoplasmic organelles.

Figure: Structure of a prokaryotic cell-bacteria

Structure of Bacteria:
(i) Plasma membrane- It is an ultra thin membrane 6-8 nm thick, chemically comprised of
molecules of lipids and proteins, arranged in a fluid mosaic pattern. Infoldings in it gives rise to
two main types of structures:
(a) Mesosomes- (Also known as Chondriods); are extensions involving complex whorls of
convoluted membranes. They increase surface area of plasma membrane and enzymatic contents.
(b) Chromatophores- These are photosynthetic pigment- bearing membranous structures of
photosynthetic bacteria and are present as vesicles, thylakoids, tubes etc.
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(ii) Cell Wall- It is strong and rigid and covers plasma membrane to provide chemical protection
and characteristic shape of bacteria. It is made up of peptidoglycan and contains muramic acid.

(iii) Capsule- In some bacteria, cell wall is surrounded by an additional slime or gel layer called
capsule that acts as protective layer against viruses and phagocytes.
(iv) Cytoplasm- It is the ground substance surrounded by plasma membrane and is site of all
metabolic activities of bacteria. It consists of water, proteins, enzymes, different types of RNA
molecules and reserve materials like glucogen, volutin and sulphur. The dense nuclear areas of
cytoplasm contain 70S ribosomes granules, composed of RNA and protein at the site of protein
synthesis.

(v) Nucleoids- The nuclear membrane includes a single, circular and double stranded DNA
molecule often called as bacterial chromosome. It is not separated by nuclear membrane and is
usually concentrated in a specific clear region of the cytoplasm called nucleoid. It has no
ribosomes, nucleolus and histone proteins.

(vi) Plasmids – Many species of bacteria may also carry extrachromosomal genetic elements in
the form of small, circular, and closed DNA molecules called plasmids. They produce
antibiotically active protein or colicins which inhibit the growth of other bacterial strain in their
vicinity. They may also act as sex or fertility factors (F factor) which stimulate bacterial
conjugation. R factors are also plasmid carrying genes for resistance to drugs.

(vii) Flagella- Many bacteria are motile and contain one or more flagella for cellular locomotion.
They are 15-20nm in diameter and up to 20µm long. e.g., E.coli etc

Eukaryotic Cell
The Eukaryotic cells are essentially two envelope systems, and they are much larger than
prokaryotic cells. Secondary membranes envelop the nucleolus and other internal organelles. The
Eukaryotic cells are true cells which occur in the plants (from algae to angiosperms) and the animal
(from Protozoa to mammals). Though the Eukaryotic cells have different shape, size, and
physiology; all the cells are typically composed of plasma membrane, cytoplasm and its organelles,
viz. Mitochondria, Endoplasmic reticulum, Ribosomes, Golgi apparatus etc; and a true nucleus.
The nuclear contents, such as DNA, RNA, Nucleoproteins and Nucleolus remain separated from

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the Cytoplasm by the thin perforated nuclear membrane.

Figure: Structure of a Eukaryotic cell

Prokaryotes Eukaryotes
Nucleus Absent Present
Membrane-bound Absent Present
organelles
Cell structure Unicellular Mostly multicellular; some
unicellular
Cell size Smaller (0.1-5 Larger (10-100 μm)
μm)
Complexity Simpler More complex
DNA Form Circular Linear
Examples Bacteria, archaea Animals, plants, fungi, protists

Structure:
1. Cell Wall: The outermost structure of most plant cells is a dead and rigid layer called cell wall. It
is mainly composed of carbohydrates such as cellulose, pectin hemicelluloses and lignin and
certain fatty substances like waxes. The cell wall which is formed immediately after the division
of cell, constitute the primary cell wall. The plant cell wall is multi-layered and consists of up to
three sections. From the outermost layer of the cell wall, these layers are identified as the middle
lamella, primary cell wall, and secondary cell wall. While all plant cells have a middle lamella
and primary cell wall, not all have a secondary cell wall.

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Figure: Structure of a cell wall

Functions-

A major role of the cell wall is to form a framework for the cell to prevent over expansion. Cellulose
fibers, structural proteins, and other polysaccharides help to maintain the shape and form of the cell.
Additional functions of the cell wall include:

• Support: The cell wall provides mechanical strength and support. It also controls the direction of
cell growth.
• Withstand turgor pressure: Turgor pressure is the force exerted against the cell wall as the
contents of the cell push the plasma membrane against the cell wall. This pressure helps a plant to
remain rigid and erect, but can also cause a cell to rupture.
• Regulate growth: The cell wall sends signals for the cell to enter the cell cycle in order to divide
and grow.
• Regulate diffusion: The cell wall is porous allowing some substances, including proteins, to pass
into the cell while keeping other substances out.
• Communication: Cells communicate with one another via plasmodesmata (pores or channels
between plant cell walls that allow molecules and communication signals to pass between
individual plant cells).
• Protection: The cell wall provides a barrier to protect against plant viruses and other pathogens.
It also helps to prevent water loss.
• Storage: The cell wall stores carbohydrates for use in plant growth, especially in seeds.

(i) Plasma Membrane: Every kind of animal cell is bounded by a living, extremely thin and
delicate membrane called Plasma lemma, cell membrane or plasma membrane. In plant calls
plasma membrane occurs just inner to cell wall, bounding the cytoplasm. The plasma membrane
exhibits a tri- laminar structure with a translucent layer sandwiched between two dark layers.
The plasma membrane is selectively permeable membrane; its main function is to control
selectively the entrance and exit of materials. This allows then cell to maintain a constant internal
environment (Homeostasis). Molecules of water, oxygen, carbon-dioxide, glucose etc., are
transported across the plasma membrane takes place by various means such as osmosis, diffusion,
and active transportation. The plasma membrane consist of mainly lipids which form lipid bi-
layers and different kinds of proteins. The proteins can be integral and peripheral proteins. In case
of the integral proteins, the proteins pass through both the bi-layers and peripheral proteins are
attached only to one lipid bi-layer. The presence of proteins provide semi-permeable nature to the
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plasma membrane. The plasma membrane are highly dynamic structures which undergo constant
changes in their structures in accordance to the changes in the environment or intracellular
activities.

Functions of Plasma membrane-


Every cell in our body is surrounded by a semipermeable membrane that serves several important
functions; it creates a protective barrier that prevents toxins from entering and prevents the
spontaneous movement of molecules out of the cell. In addition, the cell membrane also acts in signal
transduction, energy storage and transport.
Properties of Plasma membrane
(1) Cell membranes are thin enclosures that form closed boundaries.
(2) Cell membranes are made up of lipids, proteins and carbohydrates.
(3) Cell membranes consists of a phospholipid bilayer.
(4) Cell membranes are held together by non-covalent interactions
(5) Membranes are fluid-like structure.
(6) Proteins diversity the functionality of cell membranes.
(7) Membranes have polarity.
(8) Membranes are asymmetrical structures.
(9) Membranes are amphipathic in nature

Figure: Plasma membrane structure

2. Cytosol/ Cytoplasm: The plasma membrane is followed by the colloidal organic fluid called
matrix or cytosol. The cytosol is aqueous part of cytoplasm and nucleoplasm. Cytosol is
particularly rich in differentiation cells and many fundamental properties of cells are because of
this part of cytoplasm. The cytosol serves to dissolve or suspend the great variety of small
molecules concerned with cellular metabolism, e.g., glucose amino acids, nucleotides, vitamins,
minerals, oxygen. In all type of cells, cytosol contains the soluble proteins and enzymes which
form 20-25 % of the total protein content of the cells. In many types of cells, the cytosol is
differentiated into two parts:
(a) Ectoplasm or cell cortex is the peripheral layer of cytosol which is relatively non granular,
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viscous, clear and rigid.
(b) Endoplasm is the inner portion of cytosol which is granular and less viscous.

Cytoskeleton and Microtrabecular Lattice


The cytosol of cells also contains fibers that help to maintain cell shape and mobility and that
probably provide anchoring points for the other cellular structures. These fibers are called
cytoskeleton. At least three general classes of such fibers have been identified.
1- The thickest are the microtubules (20 nm in diameter) which consists primarily of the tubulin
protein. The function of microtubules is the transportation of water, ions or small molecules,
cytoplasmic streaming (cyclosis), and the formation of fibers or asters of the mitotic or meiotic
spindle during cell division.
2- The thinnest are the microfilaments (7 nm in diameter) which are solid and are solid and are
principally formed of actin protein.
3- The fibers of middle order are called the intermediate filaments (IFs) having a diameter of 10
nm. They have been classified according to their constituent protein such as desmin filaments,
keratin filament, Neurofilaments, vimentin and glial filaments.

(i) Cytoplasmic structures: In the cytoplasmic matrix certain non-living and living structures
remain suspended. The non living structures are called paraplasm and inclusion, while the living
structures can be studied under the following headings:

Cytoplasmic Inclusion
The stored food and secretory substances of the cell remain suspended in the cytoplasmic matrix
in the form of refractile granules forming the cytoplasmic inclusion. The cytoplasmic inclusion
involves oil drops, yolk granules, triacylglyerol and starch grains.

Cytoplasmic Organelles
Besides the separates fibrous systems cytoplasm is coursed by a multitude of internal membranous
structures, the organelles. Cytoplasmic organelles performed specialized tasks:Generation of energy
in the form of ATP molecules in Mitochondria; formation and storage of carbohydrates in plastids;
protein synthesis in rough endoplasmic reticulum; lipid synthesis in soft endoplasmic reticulum;
secretion by Golgi complex etc.

Endoplasmic Reticulum (ER): Within the cytoplasm of most animals cells in an extensive network
of membrane – limited channels, collectively called Endoplasmic reticulum. The outer surface of
rough endoplasmic reticulum has attached ribosomes, where as smooth endoplasmic reticulum don‘t
have. Functions of smooth ER include lipid metabolism (Both catabolism and anabolism)
glycogenolysis (degradation of glycogen) and drug detoxification.
On their membranes, rough ER contain certain ribosomes – specific, transmembrane
glycoprotein‘s called ribophorins I & II, to which are attached the ribosomes while engaged in
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polypeptide synthesis. Rough ER pinches off certain tiny protein- filled vesicles which ultimately
get fused to Cis-Golgi. RER also synthesize membrane and glycoproteins which are co
translationally inserted into rough ER membranes. Thus ER is the site of biogenesis of cellular
membranes.

General features
1. The ER is a system of membranous tubules and sacs
2. The primary function of the ER is to act as an internal transport system, allowing molecules
to move from one part of the cell to another
3. The quantity of ER inside a cell fluctuates, depending on the cell's activity. Cells with a lot
include secretory cells and liver cells
4. They take part in post-transa
5. The rough ER is studded with 80s ribosomes and is the site of protein synthesis. It is an
extension of the outer membrane of the nuclear envelope, so allowing mRNA to be
transported swiftly to the 80s ribosomes, where they are translated in protein synthesis
6. The smooth ER is where polypeptides are converted into functional proteins and where
proteins are prepared for secretion. It is also the site of lipid and steroid synthesis, and is
associated with the Golgi apparatus. Smooth ER has no 80s ribosomes and is also involved in
the regulation of calcium levels in muscle cells, and the breakdown of toxins by livercells
7. Both types of ER

Figure: Endoplasmic reticulum

Golgi Apparatus: It is cup shaped organelle which is located near the nucleus in many
typeof cells. Golgi apparatus consists of a set of smooth cisternae (i.e. close fluid –filled
flattened membranous sacs or vesicles) which often are stacked together in parallel rows. It
is surrounded by spherical membrane bound vesicles which appear to transport proteins to
and from it.
Golgi apparatus consist of at least 3 distinct classes of cisternae: Cis golgi, median golgi
and trans Golgi. Synthesized proteins appear to move in the following direction: Rough
ER cis Golgi Median Golgi Trans Golgi secretory vesicles cortical granules
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Plant cells may contain freely distributed subunits of Golgi apparatus, called Dictyosome.
Generally, Golgi apparatus perform the following functions:
1. Packaging of secretory materials.
2. Synthesis of certain polysaccharides and glycolipids.
3. Formation of acrosome of the spermatozoa.

General features
1. The Golgi apparatus is the processing, packaging and secreting organelle of the cell, so it is
much more common in glandular cells.
2. The Golgi apparatus is a system of membranes, made of flattened sac-like structures called
cisternae.
3. It works closely with the smoother, to modify proteins for export by the cell.

Figure : Golgi apparatus

Lysosomes: The cytoplasm of animals cells contains many tiny, spherical or irregular shape,
membrane bounded vesicles known as lysosomes. They digest the material taken in by endocytosis,
part of cells and extra cellular substances. Lysosomes have a high acidic medium (pH 5) and its
acidification depends upon ATP dependent proton pumps which are present in lysosomes membrane.
Lysosomes exhibits great polymorphism i.e. there is following three types of lysosomes: primary
lysosomes (storage granules) secondary lysosomes (digestive vacuoles); residual bodies. The
lysosomes of plant cells are membrane bounded storage granules containing hydrolytic digestive
enzymes‘ large vacuoles of parenchymatous cells of corn seedlings, proteins or aleurone bodies and
other seeds.

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General features
1. Lysosomes are small spherical organelles that enclose hydrolytic enzymes within a single
membrane
2. Lysosomes are the site of protein digestion – thus allowing enzymes to be re-cycled when they
are no longer required. They are also the site of food digestion in the cell, and of bacterial
digestion in phagocytes
3. Lysosomes are formed from pieces of the Golgi apparatus that break off
4. Lysosomes are common in the cells of Animals, Protoctista and even Fungi, but rare in
plants.

Figure: Types of lysozyme

Cytoplasmic Vacuoles: The cytoplasm of many plant and some animals‘ cell contain numerous
small or large-sized hollow, liquid-filled structures, the vacuoles .The vacuoles of animals are
bounded by a lipoproteinous membrane and their function is the storage, transmission of the
materials and the maintenance of internal pressure of cell. The vacuoles of plants are bounded by
a single, semi permeable membrane known as Tonoplast. The primary function of vacolules is
storage of food in the form of glycogen and are present in higher quantity and size in plant cells

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Figure: Structure of vacoules

Peroxisomes: These are tiny circular membrane bound organelles containing a crystal core of
enzymes. These enzymes are required by peroxisomes in detoxification activity. i.e., in the
metabolism or production and decomposition, of hydrogen peroxide or H2O2 molecules which
are produced during neutralization of certain superoxides- the end products of mitochondrial or
cytosolic reactions. In green leaves of plants peroxisomes carry out the process of photorespiration.
Primarily, it contains oxidase and catalase enzymes

Figure: Structure of Peroxisomes

Mitochondria: Mitochondria are oxygen consuming ribbon shaped cellular organelles of


immense importance. Each Mitochondria is bounded by two unit membranes, the outer
Mitochondria membrane resembles more with the plasma membrane in structure and chemical
composition. It contains Porins, proteins that render the membrane permeable to molecule having
molecular weight as high as 10,000. Inner Mitochondrial membrane is rich in many enzymes,
coenzymes another component of electron transport chain. It also contain proton pumps and many

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Permease proteins for the transport of various molecules so such as citrates, ADP, Phosphate &
ATP.
Inner Mitochondria membrane gives out finger-like out growths (Cristae) towards the lumen of
Mitochondrion. Mitochondrial matrix which is the liquid (colloidal) area in circled by the inner
membrane contains the soluble enzyme of Krebs cycle which completely oxidized the acetyl-CoA to
produce CO2, H2O, hydrogen ions. Hydrogen ions reduce the molecules of NAD and FAD, both of
which can pass on hydrogen ions to reparatory or electron transport chain where oxidative
phosphorylation takes place to generate energy rich molecules. Mitochondria actas the “Power House
of Cells”. Since Mitochondria can synthesize 10% of their proteins in their own protein –synthetic
machinery, they are considered as semi autonomous organelles.

Figure: structure of mitocondria

Functions:
1. The mitochondria helps in thermolysis
2. The mitochondria is involving in Ca2+ ions sequestration
3. The mitochondria generates the energy in the form of ATP through electron transport
chain (ETC cycle)
4. The mitochondria takes part in peptidy tranferase

Plastids: Plastids are double membrane organelles which are found in plant cells only. They are
usually spherical or discoidal in shape and their average size is 4 to 6 µm. A plastid shows two
distinct regions-grana and stroma. Grana are stacks of membrane-bound, flattened, discoid sacs
containing chlorophyll molecules. These molecules are responsible for the production of food by
the process of photosynthesis.
They are, therefore, called "Kitchen of the cell". They are the main functional units of the
chloroplast. The homogenous matrix in which Grana are embedded is known as Stroma. A variety
of photosynthetic enzymes and starch grains are present in the Stroma. The Stroma is colourless,
whereas the Grana contain the pigments. Plastids are living and multiply by division of the pre-
existing plastids called Proplastids.
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Functions
1. By trapping solar energy, green plastids manufacture food through photosynthesis.
2. Chromoplasts provide colored to various flowering parts.
3. Leucoplasts help in storage of protein, starch and oil.

Ribosomes: They are dense, rounded, granular and smallest known electron microscopic
Ribonucleoprotein (RNP) particles attached either on RER or floating freely in the cytoplasm. These
are the site of protein synthesis. They may exist either in free state in cytosol or attached to RER.
Ribosomes in eukaryotes have sedimentation coefficient of about 80S and are composed of 2 subunits
namely 40S and 60S, and prokaryotes have 70S and are composed of 2 subunits namely 30S and
50S.

Figure: Ribosomes of Prokaryotic and Eukaryotic cell

General features
1. Unlike most other organelles, ribosomes are not surrounded by a membrane.
2. Ribosomes are the site of protein synthesis in a cell.
3. They are the most common organelles in almost all cells.
4. Some are free in the cytoplasm (Prokaryotes) others line the membranes of rough
endoplasmic reticulum (rough ER).
5. They exist in two sizes: 70S are found in all Prokaryotes, chloroplasts and mitochondria,
suggesting that they have evolved from ancestral Prokaryotic organisms. They are free- floating.
While 80S found in all eukaryotic cells – attached to the rough ER (they are ratherlarger). Here "S"
stand as a Svedberg coefficient or unit.

Cytoskeletal Structures: Many eukaryotes have long slender motile cytoplasmic projections,
called flagella, or similar structures called cilia. Flagella and cilia are sometimes referred to as
undulipodia, and are variously involved in movement, feeding, and sensation. They are composed
mainly of tubulin. These are entirely distinct from prokaryotic flagella. They are supported by a
bundle of microtubules arising from a basal body, also called a Kinetosome or Centrioles,
characteristically arranged as nine doublets surrounding two singlets. Flagella also may have hairs,
or Mastigoneme, and scales connecting membranes and internal rods. Their interior is continuous
with the cell's cytoplasm.
Microfilament structures composed of actin and actin binding proteins, e.g., α-actinin,

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fimbrin, filamin are present in submembranous cortical layers and bundles, as well. Motorproteins
of microtubules, e.g., dynein or kinesin and actin, e.g., myosins provide dynamiccharacter of the
network.
Centrioles are often present even in cells and groups that do not have flagella, but conifers
and flowering plants have neither. They generally occur in groups of one or two, called kinetids
that give rise to various microtubular roots. These form a primary component of the cytoskeletal
structure, and are often assembled over the course of several cell divisions, with one flagellum
retained from the parent and the other derived from it. Centrioles may also be associated in the
formation of a spindle during nuclear division.
The significance of cytoskeletal structures is underlined in the determination of shape of
the cells, as well as their being essential components of migratory responses like chemo-taxis and
Chemokinesis. Some protists have various other microtubule-supported organelles. These include
the radiolaria and heliozoa, which produce axopodia used in flotation or to capture prey, and the
haptophytes, which have a peculiar flagellum-like organelle called the haptonema.

General features
1. Just as your body depends on your skeleton to maintain its shape and size, so a cell needs
structures to maintain its shape and size.
2. In animal cells, which have no cell wall, an internal framework called the cytoskeleton
maintains the shape of the cell, and helps the cell to move.
3. The cytoskeleton consists of two structures: a) microfilaments (contractile). They are made of
actin, and are common in motile cells. b) microtubules (rigid, hollow tubes – made of tubulin).
4. Microtubules have three functions:
(a) To maintain the shape of the cell.
(b) To serve as tracks for organelles to move along within the cell.
(c) They form the Centrioles.

Nucleus: The nucleus is a membrane-enclosed organelle found in eukaryotic cells. Eukaryotes


usually have a single nucleus, but a few cell types, such as mammalian red blood cells, have no
nuclei, and a few others have many.
Cell nuclei contain most of the cell's genetic material, organized as multiple long linear
DNA molecules in complex with a large variety of proteins, such as histones, to form
chromosomes. The genes within these chromosomes are the cell's nuclear genome and are
structured in such a way to promote cell function. The nucleus maintains the integrity of genes and
controls the activities of the cell by regulating gene expression—the nucleus is, therefore, the
control center of the cell. The main structures making up the nucleus are the nuclear envelope, a
double membrane that encloses the entire organelle and isolates its contents from the cellular
cytoplasm, and the nuclear matrix (which includes the nuclear lamina), a network within the
nucleus that adds mechanical support, much like the cytoskeleton, which supports the cell as a
whole.
Because the nuclear membrane is impermeable to large molecules, nuclear pores are required that
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regulate nuclear transport of molecules across the envelope. The pores cross both nuclear
membranes, providing a channel through which larger molecules must be actively transported by
carrier proteins while allowing free movement of small molecules and ions. Movement of large
molecules such as proteins and RNA through the pores is required for both gene expression and
the maintenance of chromosomes. Although the interior of the nucleus does not contain any
membrane-bound sub compartments, its contents are not uniform, and a number of sub-nuclear
bodies exist, made up of unique proteins, RNA molecules, and particular parts of the
chromosomes. The best-known of these is the nucleolus, which is mainly involved in the assembly
of ribosomes. After being produced in the nucleolus, ribosomes are exported to the cytoplasm
where they translate mRNA.

Figure: Eukaryotic nucleus

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The Nucleus is normally the largest organelle within a Eukaryotic cell.


1. Prokaryotes have no nucleus, having a nuclear body instead. This has no membrane
and a loop of DNA (and no chromatin proteins).
2. The nucleus contains the cell‘s chromosomes (human 46, fruit fly 6, fern 1260)
which are normally uncoiled to form a chromatin network, which contain both
linear DNA and proteins, known as histones. These proteins coil up (dehydrate)
at the start of nuclear division, when the chromosomes first become visible.
3. Whilst most cells have a single nucleus some cells (macrophages, phloem
companion cells) have more than one.
4. Fungi have many nuclei in their cytoplasm, they are coenocytic (common
cytoplasm throughout).
5. The nucleus is surrounded by a double membrane called the nuclear envelope.
6. The nuclear envelope has many nuclear pores through which mRNA, and proteins can
pass.
7. Most nuclei contain at least one nucleolus (plural, nucleoli). The nucleoli are,
where ribosomes are synthesized. Ribosomes translate mRNA into proteins.
8. When a nucleus prepares to divide, the nucleolus disappears.

The following table featuring different organelles of cell with their location,
description andfunctions.
ORGANELLE LOCATION DESCRIPTION FUNCTION
Support (grow tall) protection
Cell wall Plant, not animal Outer layer rigid, strong, allows H2O, O2, CO2 to pass into
stiff made of cellulose
and out of cell

Plant - inside cell wall Support protection controls


Cell membrane Both plant/animal animal - outer layer; movement of materials in/out of
cholesterol selectively cell barrier between cell and its
permeable environment maintains homeostasis

Nucleus Both plant/animal Large, oval Controls cell activities

Nuclear Surrounds nucleus Controls movement of materials


Both plant/animal
membrane selectively permeable in/out of nucleus
Clear, thick, jellylike
Cytoplasm Both plant/animal material and organelles Supports /protects cell organelles
found inside cell
membrane
Endoplasmic
reticulum Both plant/animal Network of tubes or Carries materials through cell
membranes
(E.R.)
Small bodies free or
Ribosome Both plant/animal Produces proteins
attached to E.R.

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Department of Biotechnology Biology for Engineers (S4CCA01)

Bean-shaped with inner Breaks down sugar molecules into


Mitochondrion Both plant/animal
membranes energy

Vacuole Plant - few/large Fluid-filled sacs Store food, water, waste (plants
animal - small need to store large amounts of food)

Lysosome Plant - Small, round, with a Breaks down larger food molecules
uncommon membrane into smaller molecules digests old
animal - common cell parts

Green, oval usually


Chloroplast Plant, not animal containing chlorophyll Uses energy from sun to make food
for the plant (photosynthesis)
(green pigment)

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Department of Biotechnology Biology for Engineers (S4CCA01)

Biomolecule, any of numerous substances that are produced by cells and living organisms.
Biomolecules have a wide range of sizes and structures and perform a vast array of functions.
The four major types of biomolecules are carbohydrates, lipids, nucleic acids, and proteins.

Among biomolecules, nucleic acids, namely DNA and RNA, have the unique function
of storing an organism’s genetic code—the sequence of nucleotides that determines
the amino acid sequence of proteins, which are of critical importance to life on Earth.
There are 20 different amino acids that can occur within a protein; the order in which
they occur plays a fundamental role in determining protein structure and function.
Proteins themselves are major structural elements of cells. They also serve as
transporters, moving nutrients and other molecules in and out of cells, and
as enzymes and catalysts for the vast majority of chemical reactions that take place in
living organisms. Proteins also form antibodies and hormones, and they
influence gene activity.

Intrinsic proteins penetrate and bind tightly to the lipid bilayer, which is made up largely of
phospholipids and cholesterol and which typically is between 4 and 10 nanometers (nm; 1 nm
= 10−9 metre) in thickness. Extrinsic proteins are loosely bound to the hydrophilic (polar)
surfaces, which face the watery medium both inside and outside the cell. Some intrinsic
proteins present sugar side chains on the cell's outer surface.

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Department of Biotechnology Biology for Engineers (S4CCA01)

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Department of Biotechnology Biology for Engineers (S4CCA01)

DNA packaging into chromatin and chromosome


DNA wraps around proteins called histones to form units known as nucleosomes. These units
condense into a chromatin fibre, which condenses further to form a chromosome.(more)

All biomolecules share in common a fundamental relationship between structure and function,
which is influenced by factors such as the environment in which a given biomolecule occurs.
Lipids, for example, are hydrophobic (“water-fearing”); in water, many spontaneously arrange
themselves in such a way that the hydrophobic ends of the molecules are protected from the
water, while the hydrophilic ends are exposed to the water. This arrangement gives rise
to lipid bilayers, or two layers of phospholipid molecules, which form the membranes of cells
and organelles. In another example, DNA, which is a very long molecule—in humans, the
combined length of all the DNA molecules in a single cell stretched end to end would be about
1.8 metres (6 feet), whereas the cell nucleus is about 6 μm (6 10-6 metre) in diameter—has a
highly flexible helical structure that allows the molecule to become tightly coiled and looped.
This structural feature plays a key role in enabling DNA to fit in the cell nucleus, where it
carries out its function in coding genetic traits.

Carbohydrates
The term carbohydrate is a combination of the “hydrates of carbon”. They are also known as
“Saccharides”, a derivation of the Greek word “Sakcharon”, which means sugar. “Optically
active polyhydroxy aldehydes or ketones or substances formed during hydrolysis are known as
carbohydrates”.Few of the most common carbohydrates that we come across in our daily lives
are in the form of sugars. These sugars can be in the form of Glucose, Sucrose, Fructose,
Cellulose, Maltose etc. The general formula for carbohydrates is Cx(H2O)y

Classification of Carbohydrates:

The main classification of carbohydrates is done based on hydrolysis. This classification is as


follows:

1. Monosaccharides are the more straightforward form of carbohydrates that cannot be


hydrolyzed into a more straightforward unit of polyhydroxy aldehyde or ketone called
monosaccharides. Approximately twenty monosaccharides are known to occur in
nature. For example, glucose and fructose. Their general formula is (CH2O)n. Some
examples are glucose, Ribose, etc.
2. Oligosaccharides: Carbohydrates that, upon hydrolysis yield, two to ten smaller units
or monosaccharides are called oligosaccharides. They are a large category and further
divided into various subcategories.
3. Disaccharides: A further classification of oligosaccharides, gives two units of different
or the same monosaccharides on hydrolysis. One example, sucrose on hydrolysis gives
one molecule of glucose and fructose each. In contrast, maltose on hydrolysis gives two
molecules of only glucose.
4. Trisaccharides: Carbohydrates that on hydrolysis give three molecules of
monosaccharides, identical or different. An example is Raffinose.
5. Tetrasaccharides: As the name suggests, this carbohydrate on hydrolysis gives four
molecules of monosaccharides. Stachyose is an example.
6. Polysaccharides: The last and final category of carbohydrates. These give a very large
number of monosaccharides when they go through hydrolysis. These carbohydrates are
not sweet and are also known as non-sugars. Some common examples are starch,
glycogen etc.

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Department of Biotechnology Biology for Engineers (S4CCA01)

Importance of Carbohydrates:

• They are responsible for storing chemical energy in living organisms. You must hear it
all the time when athletes carbo-load before a game. This is to provide them with extra
energy. They are also an essential constituent for supporting tissues in plants and even
in some animals.
• Photosynthesis is a process by which plants use solar energy to produce food for
themselves. With this process, plants fix CO2 and synthesize carbohydrates.

Figure: Structure of carbohydrates

Nucleic acids

The particles in the nucleus of the biological cell responsible for heredity are called
chromosomes which are made up of proteins and other biomolecules called nucleic acids.
Nucleic acids are polymers which are present in all human bodies.

• Nucleic acids play an essential role in the development and reproduction of every life
form.
• Nucleic acid contains the elements carbon-oxygen, nitrogen and phosphorus.
• They have nucleotides as their repeating units.
Two types of nucleic acids:

• DNA (Deoxyribonucleic acid).


• RNA (Ribonucleic acid).
Deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) are two major types of nucleic
acids. DNA and RNA are responsible for inheriting and transmitting specific characteristics
from one generation to the other.

Deoxyribonucleic Acid (DNA):

• Chemically, DNA comprises a pentose sugar, phosphoric acid and a few cyclic bases
containing nitrogen.
• The sugar unit present in DNA molecules is β-D-2-deoxyribose.
• The cyclic bases that have nitrogen-containing in them are Adenine (A), guanine (G),
thymine (T) and cytosine(C).
• These bases and their configuration in the molecules of DNA play an essential role in
storing information from one generation to the next.
• DNA has a double-strand helical structure in which the strands complement each other.
Ribonucleic Acid (RNA):

• The RNA molecule is also composed of phosphoric acid, a pentose sugar and a few
cyclic bases containing nitrogen.

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Department of Biotechnology Biology for Engineers (S4CCA01)

• RNA has β-D-ribose in it as the sugar unit.


• The heterocyclic bases available in RNA are Adenine (A), guanine (G), cytosine(C)
and uracil (U).
• In RNA, the fourth base varies from that of DNA.
• The RNA commonly consists of a single strand which sometimes folds back; that
results in a double helix structure.
There are three different types of RNA molecules, each having a specific function:

1. Messenger RNA (mRNA).


2. Ribosomal RNA (rRNA).
3. Transfer RNA (t-RNA).

Nucleotides contain three chemical components:

• A heterocyclic base.
• A five-carbon sugar moiety.
• A phosphate group.
Structure of Nucleic acids:

1. Nitrogen-containing heterocyclic base: Purines and pyrimidines are two types of


heterocyclic bases. For example, Adenine and guanine are purines. Cytosine, thymine,
and uracil are pyrimidines.
2. Sugars: The two types of sugars are RNA and DNA.
iii. Phosphate group: Nucleotides are joined by these linkages.

1. Nucleoside: A nucleoside unit is produced when a nitrogen base is attached to a sugar


molecule.
Base + sugar = nucleoside.

1. Nucleotide: When a nitrogen base is attached to a sugar molecule and phosphate, the
unit forms a nucleotide.
Base+Sugar+phosphate → nucleotide.

Functions of nucleic acids


• Nucleic acids are responsible for transmitting inherent characteristics from parent to
offspring. They are also responsible for the synthesis of protein in our bodies.
• DNA fingerprinting is a method that is used by forensic experts to determine paternity.
This method is also used for the identification of criminals. It has also played a
significant role in biological evolution and genetics studies.
• Replication: It is the characteristics of a bio-molecule to synthesize different molecules.
For example, DNA has a specific property to replicate itself.
• Protein synthesis: Genetic information collected in DNA in a specific base sequence is
expressed in the form of a specific base sequence.
• Gene and genetic code: Every segment of DNA molecule that codes for a specific
protein or a polypeptide, known as the relationship between nucleotides triplets and the
amino acids, is called the genetic code. This is what forms gene and genetic code.
• Mutation: A chemical process in a DNA molecule leads to the synthesis of proteins
with a changed amino acid sequence. Radiation, viruses or chemical agents cause these

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Department of Biotechnology Biology for Engineers (S4CCA01)

changes. Special enzymes replicate most changes in DNA in the cell, but if there is a
failure to repair by the enzymes, then it can cause mutation.

Proteins:

Proteins are higher in molecular weight, complex bio-polymers of alpha-amino acids found in
all living organisms. They occur in all parts of the body and form the fundamental basis of the
structure and functions of life. The term ‘Protein’ is derived from the Greek word ‘Protein’,
which means ‘Primary importance’. Proteins are the amplest biomolecules of the living cell.
The primary sources of proteins are milk, cheese, pulses, peanuts, fish etc. All living systems
comprise biomolecules with high molecular mass, called amino acids.

Amino acids:

These acids are the building block units of proteins. These are the organic compounds which
contain amino as well as carboxyl functional groups known as amino acids. Depending upon
the relative position of the amino group concerning the COOH group, amino acids are
Classified into alpha-beta, gamma delta and so on. Hydrolysis of proteins gives only alpha-
amino acids represented as:

• The above unit may be connected to any carbon atom other than the -COOH group.
• The amino acids can also be classified based on their need and availability in the human
body.
Essential Amino Acids:

These acids cannot be synthesized in our bodies and are essential amino acids that must be
taken through diet. We must depend on food sources to obtain these amino acids. Some of the
primary essential Amino Acids are as below:

• Leucine.
• Isoleucine.
• Lysine.
• Threonine.
• Methionine.
• Phenylalanine.
• Valine.
• Tryptophan.
• Histidine (conditionally essential).
Non-Essential Amino acids:

These acids are synthesized in our bodies by themselves. So we need not rely on external
sources for them. They are produced in our bodies and also obtained from protein breakdowns.

Properties of Amino Acids:

We have seen the overall structure and types of amino acids. Based on this information, we can
arrive at the properties of amino acids.

• Each amino acid has an acidic and fundamental group, as seen from its structure.
Because of this reason they behave similar to salts.

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Department of Biotechnology Biology for Engineers (S4CCA01)

• They exist as dipolar ions.


• Any amino acid in the dry state exists in crystalline form.
• The NH2 group exists as a cation, and the COOH group exists as an anion. This dipolar
ion has a unique name, “Zwitterions’.
• In an aqueous solution, alpha-amino acids exist in equilibrium between a cationic form,
an anionic form and a dipolar ion.
• The isoelectric point (IEP) is the pH point at which the concentration of zwitterions is
the highest, and the concentration of cationic and anionic forms is equal.
• This specific point is definite for every α-amino acid.
• They are generally water-soluble and also have high melting points.

Structure of proteins:

• Amino acids exist as a zwitterion, which is dipolar.


• The fundamental nature of the zwitterion is due to the -COO– ion.
• The acidic character of the zwitterion is due to the -NH3+ group.
Peptide linkage:

When two or more amino acids are attached, the resulting -CO-NH- link is termed peptide
linkage of the peptide bond.

Figure: the various conformations of proteins


Enzymes
Enzymes are the biological macromolecules which speed up the rate of biochemical reactions
without undergoing any change. They are also called as biological catalysts. An enzyme is a highly
selective catalyst that greatly accelerates both the rate and specificity of metabolic reactions.
Enzymes are biological catalysts made up of large protein molecules. They speed up the chemical
reactions inside the cell. The enzyme is made up of a combination of amino acids which for a chain
of polypeptides between each other. Enzymes are similar to other chemical catalysts. They
participate in the reaction without getting affected. In other words, they speed up the chemical
reactions inside the cells without getting consumed.
They are also addressed as biocatalysts. All enzymes are catalysts but not all catalysts are enzymes.

Enzymes and catalysts both affect the rate of a reaction. In fact, all known enzymes are catalysts,
but not all catalysts are enzymes. The difference between catalysts and enzymes is that enzymes

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Department of Biotechnology Biology for Engineers (S4CCA01)

are largely organic in nature and are biocatalysts, while non-enzymatic catalysts can be inorganic
compounds. Neither catalysts nor enzymes are consumed in the reactions they catalyze.
Comparison of chemical catalyst and enzymes

Catalyst Enzyme
Function Catalysts are substances that Enzymes are proteins that
increase or decrease the rate increase rate of chemical
of a chemical reaction but reactions converting
remain unchanged. substrate into product.
Molecular weight Low molecular weight High molecular weight
compounds. globular proteins
Types There are two types of There are two types of
catalysts – positive and enzymes - activation
negative catalysts. enzymes and inhibitory
enzymes.
Nature Catalysts are simple Enzymes are complex
inorganic molecules. proteins.
Reaction type Catalysts act on physical Enzymes act on biochemical
reactions reactions
Alternate terms Inorganic catalyst. Organic catalyst or bio
catalyst.
Reaction rates Typically slower Several times faster
Specificity They are not specific and Enzymes are highly specific
therefore end up producing producing large number of
residues with errors good residues
Active site of the enzyme
The active site of an enzyme is the region that binds the substrate and converts it into product. It is
usually a relatively small part of the whole enzyme molecule and is a three-dimensional entity
formed by amino acid residues that can lie far apart in the linear polypeptide chain. The active site
is often a cleft or crevice on the surface of the enzyme that forms a predominantly nonpolar
environment which enhances the binding of the substrate. The substrate(s) is bound in the active
site by multiple weak forces (electrostatic interactions, hydrogen bonds, van der Waals bonds,
hydrophobic interactions, and in some cases by reversible covalent bonds. The properties and
spatial arrangement of the amino acid residues forming the active site of an enzyme will determine
which molecules can bind and be substrates for that enzyme.
Mechanism of action of Enzymes
The substrate(s) is bound in the active site by multiple weak forces which result into the enzyme-
substrate complex. Once bound active residues within the active site of the enzyme act on the
substrate molecule to transform it first into the transition state complex and then into product, which
is released. The enzyme is now free to bind another molecule of substrate and begin its catalytic
cycle again.
[E]+[S] [ES] [E]+[P]
Enzyme+substrate Enzyme-substrate complex Enzyme + Product

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Department of Biotechnology Biology for Engineers (S4CCA01)

Figure: The binding of the substrate (maltose/glucose) onto the active site of the enzyme. The
structure of the substrate is complementary to the enzyme

The enzyme-substrate complex-


Lock and key model- In the lock-and-key model proposed was proposed by Emil Fischer in
1894.cAccording to the model, the shape of the substrate and the active site of the enzyme are
thought to fit together like a key into its lock. The two shapes are considered as rigid and fixed, and
perfectly complement each other when brought together in the right alignment.
Induced fit model- In the induced-fit model was proposed by Daniel E. Koshland, Jr., in 1958. It
states that the binding of substrate induces a conformational change in the active site of the enzyme.
In addition, the enzyme may distort the substrate, forcing it into a conformation similar to that of
the transition state. For example, the binding of glucose to hexokinase induces a conformational
change in the structure of the enzyme such that the active site assumes a shape that is
complementary to the substrate (glucose) only after it has bound to the enzyme.
The reality is that different enzymes show features of both models, with some complementarity
and some conformational change.

Figure: The two theories which is Lock and key model and induced fit model proposed for
enzyme-substrate interactions

Coenzymes and prosthetic groups


Many enzymes require the presence of small, non-protein units or cofactors to carry out their
reaction. Cofactors may be either one or more

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Department of Biotechnology Biology for Engineers (S4CCA01)

Isoenzyme
Isoenzymes are different forms of an enzyme which catalyze the same reaction, but which
exhibit different physical or kinetic properties, such as isoelectric point, pH optimum, substrate
affinity or effect of inhibitors. Different isoenzyme forms of a given enzyme are usually derived
from different genes and often occur in different tissues of the body. An example of an enzyme
which has different isoenzyme forms is lactate dehydrogenase (LDH) which catalyzes the
reversible conversion of pyruvate into lactate in the presence of the coenzyme NADH.
Enzymes are affected by the hydrogen ion concentration (pH) and the temperature. Enzymes
are highly specific compared to other catalysts, and each enzyme is specialized for one reactant
substance. This reactant substance is called substrate, and it is specialized for one type of
reaction or a few reactions. Enzymes lower the activation energy required to get the reaction
started. Collectively, these are the most important properties of the enzyme. Activation energy
is defined as the minimum energy required to start an reaction.

Properties of Enzymes

1. Nearly all enzymes are proteins, although a few catalytically active RNA molecules have
been identified.
2. Enzyme catalyzed reactions usually take place under relatively mild conditions
(temperatures well below 100oC, atmospheric pressure and neutral pH) as compared with
the corresponding chemical reactions.
3. Enzymes are catalysts that increase the rate of a chemical reaction without being changed
themselves in the process.
4. Enzymes are highly specific with respect to the substrates on which they act and the
products that they form.
5. Enzyme activity can be regulated, varying in response to the concentration of substrates
or other molecules.
6. They function under strict conditions of temperature and pH in the body.

Nomenclature of the enzymes

Many enzymes are named by adding the suffix ‘-ase_’ _to the name of their substrate.
However, other enzymes, such as trypsin and chymotrypsin, have names that do not denote
their substrate. Some enzymes have several alternative names. To rationalize enzyme names, a
system of enzyme nomenclature has been internationally agreed. For example. Urease is the
enzyme that catalyzes the hydrolysis of urea, and fructose-1,6-bisphosphatase hydrolyzes
fructose-1,6-bisphosphate.

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Department of Biotechnology Biology for Engineers (S4CCA01)

Classification of Enzymes

1. Oxidoreductases

Catalyze oxidation-reduction reactions where electrons are transferred. These electrons are
usually in the form of hydride ions or hydrogen atoms. The most common name used is a
dehydrogenase and sometimes reductase is used. An oxidase is referred to when the oxygen
atom is the acceptor. Example-

2. Transferases

Catalyze group transfer reactions. The transfer occurs from one molecule that will be the donor
to another molecule that will be the acceptor. Most of the time, the donor is a cofactor that is
charged with the group about to be transferred. Example: Hexokinase used in glycolysis.

3. Hydrolases

Catalyze reactions that involve hydrolysis. It usually involves the transfer of functional groups
to water. When the hydrolase acts on amide, glycosyl, peptide, ester, or other bonds, they not
only catalyze the hydrolytic removal of a group from the substrate but also a transfer of the
group to an acceptor compound. For example: Chymotrypsin.

4. Lyases

Catalyze reactions where functional groups are added to break double bonds in molecules or
the reverse where double bonds are formed by the removal of functional groups. For example:
Fructose bisphosphate aldolase used in converting fructose 1,6-bisphospate

5. Isomerases

Catalyze reactions that transfer functional groups within a molecule so that isomeric forms are
produced. These enzymes allow for structural or geometric changes within a compound. For
example: phosphoglucose isomerase for converting glucose 6-phosphate to fructose 6-
phosphate. Moving chemical group inside same substrate.

6. Ligases

They are involved in catalysis where two substrates are ligated and the formation of carbon-
carbon, carbon-sulfide, carbon-nitrogen, and carbon-oxygen bonds due to condensation
reactions. These reactions are coupled to the cleavage of ATP.

Factors affecting the enzyme function-

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Department of Biotechnology Biology for Engineers (S4CCA01)

There are several factors that affect the speed of an enzyme’s action, such as the concentration
of the enzyme, the concentration of the substrate, temperature, hydrogen ion concentration
(pH), and the presence of inhibitors.

Vitamins:

Vitamins are organic compounds essential for the average growth of life for animals, some
bacteria and microorganisms. These are the biomolecules which are not produced by the body
and hence, need to be supplied in small amounts for necessary biological functions. Vitamins
are an essential dietary factor.

A, B, C, D, E, & K vitamins are present in various food forms.

Classification of vitamins:

Vitamins are classified into two categories:

• Water-soluble vitamins: Water-soluble vitamins are vitamin B and C complex etc.


These vitamins need to be transferred to the body from time to time.
• Fat-soluble vitamins: Vitamins only soluble in fat are called fat-soluble vitamins.
A(Retinol), D(calciferol), E(Tocopherol), and K(Phylloquinone) vitamins are soluble
in fat.
Particular vitamins are responsible for certain essential functions. Let us have a brief look at
them.

• Vitamin A: Required to enable night vision in humans. Cells require Vitamin A for the
transfusion of light.
• Vitamin B: Necessary for creating serotonin, myelin, dopamine and epinephrine. It also
lowers cholesterol levels.
• Vitamin C: Increases the immune system and helps fatigued muscles.
• Vitamin D: The formation of RNA needs Vitamin D. It also helps bones absorb calcium
to stay healthy and strong and reduces the risk of fractures
• Vitamin E has antioxidant properties that help our bodies get rid of free radicals and
assist in the formation of red blood cells.
• Vitamin K: Essential in creating some crucial proteins, Various important vitamins,
their sources and their deficiency diseases.

Name of sources Deficiency diseases


vitamins

Vitamin A Fish liver oil, carrots, butter and Xerophthalmia, Night blindness
milk

Vitamin B1 Yeast, milk, cereals, green Beri Beri


veggies

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Department of Biotechnology Biology for Engineers (S4CCA01)

Vitamin B2 egg white, milk, liver Cheilosis

Vitamin B6 Yeast, milk, cereals and grams convulsions

Vitamin B12 Meat, fish, egg and curd Pernicious

Vitamin C Citrus fruits, amla scurvy

Vitamin D Exposure to sunlight, fish Rickets

Vitamin E Vegetable oils like wheat germ Increased fragility of RBC and
oil muscular weakness

Vitamin K Green leafy vegetables Increased blood clotting time

Hormones:

Hormones are molecules which act as intracellular messengers. These are constructed by
endocrine glands in the body and are poured directly into the bloodstream, which transports
them to the site of action.

Hormones have various functions in the body. They help to adjust the balance of biological
activities in the body.

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Department of Biotechnology Biology for Engineers (S4CCA01)

Figure: the site of origin of hormones

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Department of Biotechnology Biology for Engineers (S4CCA01)

Figure: The functions of the hormones

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